Journal
JOURNAL OF VIROLOGY
Volume 80, Issue 6, Pages 3071-3077Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.80.6.3071-3077.2006
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Funding
- NIAID NIH HHS [R01 AI023173, AI-23173] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008152, T32 GM08152-18] Funding Source: Medline
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Paramyxoviruses enter cells by fusing their envelopes with the plasma membrane, a process that occurs at neutral pH. Recently, it has been found that there is an exception to this dogma in that a porcine isolate of the paramyxovirus parainfluenza virus 5 (PIV5), known as SER, requires a low-pH step for fusion (S. Seth, A. Vincent, and R. W. Compans, J. Virol. 77: 6520-6527, 2003). As a low-pH activation mechanism for fusion would greatly facilitate biophysical studies of paramyxovirus-mediated membrane fusion, we have reexamined the triggering of the PIV5 SER fusion protein. Using multiple assays, we could not find a requirement for low-pH triggering of PIV5 SER fusion. The challenge of discovering how the paramyxovirus receptor binding protein (HN, H, or G) activates the metastable fusion protein to cause membrane fusion at neutral pH remains.
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